|
Name |
Accession |
Description |
Interval |
E-value |
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
2-300 |
6.92e-136 |
|
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).
Pssm-ID: 274804 [Multi-domain] Cd Length: 304 Bit Score: 386.56 E-value: 6.92e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 2 IYTVTLNPSIDYIVRLDQVKVGSVNRMDSDDKFAGGKGINVSRVLKRLNIPNTATGFIGGFTGKFITDTLAEEEIETRFV 81
Cdd:TIGR03828 1 IYTVTLNPAIDLTIELDGLTLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEALLREEGIKTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 82 QVAEDTRINVKIK--ADQETEINGTGPTVESVQLEELKAILSSLTAE-DTVVFAGSSAKNLGNVIYKDLISLTRQTGAQV 158
Cdd:TIGR03828 81 RVPGETRINVKIKepSGTETKLNGPGPEISEEELEALLEKLRAQLAEgDWLVLSGSLPPGVPPDFYAELIALAREKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 159 VCDFEGQTLIDSLDYQPLLVKPNNHELGAIFGVKLESLDEIEKYARELLAKGAQNVIISMAGDGALLVTSDGAYFAKPIK 238
Cdd:TIGR03828 161 ILDTSGEALRDGLKAKPFLIKPNDEELEELFGRELKTLEEIIEAARELLDLGAENVLISLGADGALLVTKEGALFAQPPK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 926808626 239 GTVKNSVGAGDSMVAGFTGEFVKSKDAVEAFKWGVACGTATTFSDD--LATAEFIKETYGKVEV 300
Cdd:TIGR03828 241 GEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGtgLPDPEDIEELLPQVTI 304
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
2-299 |
3.88e-135 |
|
hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.
Pssm-ID: 274464 [Multi-domain] Cd Length: 303 Bit Score: 384.62 E-value: 3.88e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 2 IYTVTLNPSIDYIVRLDQVKVGSVNRMDSDDKFAGGKGINVSRVLKRLNIPNTATGFIGGFTGKFITDTLAEEEIETRFV 81
Cdd:TIGR03168 1 IYTVTLNPAIDLTIEVDGLTPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFTGEFIEALLAEEGIKNDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 82 QVAEDTRINVKIK--ADQETEINGTGPTVESVQLEELKAILSSLTAE-DTVVFAGSSAKNLGNVIYKDLISLTRQTGAQV 158
Cdd:TIGR03168 81 EVKGETRINVKIKesSGEETELNEPGPEISEEELEQLLEKLRELLASgDIVVISGSLPPGVPPDFYAQLIAIARKKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 159 VCDFEGQTLIDSLDYQPLLVKPNNHELGAIFGVKLESLDEIEKYARELLAKGAQNVIISMAGDGALLVTSDGAYFAKPIK 238
Cdd:TIGR03168 161 ILDTSGEALREALAAKPFLIKPNHEELEELFGRELKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKATPPK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 926808626 239 GTVKNSVGAGDSMVAGFTGEFVKSKDAVEAFKWGVACGTATTFSDDL--ATAEFIKETYGKVE 299
Cdd:TIGR03168 241 VEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGTglPDPEDVEELLDQVT 303
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
2-299 |
1.17e-134 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 383.72 E-value: 1.17e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 2 IYTVTLNPSIDYIVRLDQVKVGSVNRMDSDDKFAGGKGINVSRVLKRLNIPNTATGFIGGFTGKFITDTLAEEEIETRFV 81
Cdd:COG1105 1 ILTVTLNPALDRTYEVDELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEEGIPTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 82 QVAEDTRINVKIKAD---QETEINGTGPTVESVQLEELKAILSSLTAE-DTVVFAGSSAKNLGNVIYKDLISLTRQTGAQ 157
Cdd:COG1105 81 PIEGETRINIKIVDPsdgTETEINEPGPEISEEELEALLERLEELLKEgDWVVLSGSLPPGVPPDFYAELIRLARARGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 158 VVCDFEGQTLIDSLDYQPLLVKPNNHELGAIFGVKLESLDEIEKYARELLAKGAQNVIISMAGDGALLVTSDGAYFAKPI 237
Cdd:COG1105 161 VVLDTSGEALKAALEAGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRAKPP 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 926808626 238 KGTVKNSVGAGDSMVAGFTGEFVKSKDAVEAFKWGVACGTATTFSDD--LATAEFIKETYGKVE 299
Cdd:COG1105 241 KVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGtgLPDREDVEELLAQVE 304
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
1-286 |
8.34e-133 |
|
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.
Pssm-ID: 238570 [Multi-domain] Cd Length: 289 Bit Score: 378.41 E-value: 8.34e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 1 MIYTVTLNPSIDYIVRLDQVKVGSVNRMDSDDKFAGGKGINVSRVLKRLNIPNTATGFIGGFTGKFITDTLAEEEIETRF 80
Cdd:cd01164 1 MIYTVTLNPAIDLTIELDQLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFTGDFFEALLKEEGIPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 81 VQVAEDTRINVKIKAD--QETEINGTGPTVESVQLEELKAILSSLTAE-DTVVFAGSSAKNLGNVIYKDLISLTRQTGAQ 157
Cdd:cd01164 81 VEVAGETRINVKIKEEdgTETEINEPGPEISEEELEALLEKLKALLKKgDIVVLSGSLPPGVPADFYAELVRLAREKGAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 158 VVCDFEGQTLIDSLDYQPLLVKPNNHELGAIFGVKLESLDEIEKYARELLAKGAQNVIISMAGDGALLVTSDGAYFAKPI 237
Cdd:cd01164 161 VILDTSGEALLAALAAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRASPP 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 926808626 238 KGTVKNSVGAGDSMVAGFTGEFVKSKDAVEAFKWGVACGTATTFSDDLA 286
Cdd:cd01164 241 KVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
7-280 |
7.43e-52 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 172.14 E-value: 7.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 7 LNPSID----YIVRLDQVKVGSVNRMDSDDKFAGGKGINVSRVLKRLNIPNTATGFIGG-FTGKFITDTLAEEEIETRFV 81
Cdd:pfam00294 1 KVVVIGeaniDLIGNVEGLPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDdNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 82 QVAEDTRINVK---IKADQETEINGTGPTVESVQLEELKAILSSLTAEDTVVFAGSSAKNLGNVIYKDLISLTRQ--TGA 156
Cdd:pfam00294 81 VIDEDTRTGTAlieVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYISGSLPLGLPEATLEELIEAAKNggTFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 157 QVVCDFEGQTLIDSLDYQPL--LVKPNNHELGAIFGVKLESLDEIEKYARELLAKGAQNVIISMAGDGALLVTSDGAYFA 234
Cdd:pfam00294 161 PNLLDPLGAAREALLELLPLadLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEVHV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 926808626 235 KPI-KGTVKNSVGAGDSMVAGFTGEFVKSKDAVEAFKWGVACGTATT 280
Cdd:pfam00294 241 PAVpKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVV 287
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
4-254 |
1.66e-50 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 169.11 E-value: 1.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 4 TVTLNPSIDYIVRLDQVKVGSVNRMDSDDKFAGGKGINVSRVLKRLNIPNTATGFIG-----GFTGKFitdtlAEEEIET 78
Cdd:PRK09513 7 TITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGkdnqdGFQQLF-----SELGIAN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 79 RFVQVAEDTRINVKI--KADQETEINGTGPTVESVQLEELKA-ILSSLTAEDTVVFAGSSAKNLGNVIYKDLISLTRQTG 155
Cdd:PRK09513 82 RFQVVQGRTRINVKLteKDGEVTDFNFSGFEVTPADWERFVTdSLSWLGQFDMVAVSGSLPRGVSPEAFTDWMTRLRSQC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 156 AQVVCDFEGQTLIDSLDYQPLLVKPNNHELGAIFGVKLESLDEIEKYARELLAKGAQNVIISMAGDGALLVTSDGAYFAK 235
Cdd:PRK09513 162 PCIIFDSSREALVAGLKAAPWLVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAK 241
|
250
....*....|....*....
gi 926808626 236 PIKGTVKNSVGAGDSMVAG 254
Cdd:PRK09513 242 PPACDVVSTVGAGDSMVGG 260
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
1-270 |
4.33e-50 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 167.98 E-value: 4.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 1 MIYTVTLNPSIDYIVRLDQVKVGSVNRMDSDDKFAGGKGINVSRVLKRLNIPNTATGFIGGFTGKFITDTLaEEEIETRF 80
Cdd:PRK13508 1 MILTVTLNPSIDISYPLDELKLDTVNRVVDVSKTAGGKGLNVTRVLSEFGENVLATGLIGGELGQFIAEHL-DDQIKHAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 81 VQVAEDTRINVKI-KADQETEINGTGPTVESVQLEELKAILSSL-TAEDTVVFAGSSAKNLGNVIYKDLISLTRQTGAQV 158
Cdd:PRK13508 80 YKIKGETRNCIAIlHEGQQTEILEKGPEISVQEADGFLHHFKQLlESVEVVAISGSLPAGLPVDYYAQLIELANQAGKPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 159 VCDFEGQTLIDSL--DYQPLLVKPNNHELGAIFGVKL-ESLDEIEKYARELLAKGAQNVIISMAGDGALLVTSDGAYFAK 235
Cdd:PRK13508 160 VLDCSGAALQAVLesPYKPTVIKPNIEELSQLLGKEVsEDLDELKEVLQQPLFEGIEWIIVSLGADGAFAKHNDTFYKVD 239
|
250 260 270
....*....|....*....|....*....|....*
gi 926808626 236 PIKGTVKNSVGAGDSMVAGFTGEFVKSKDAVEAFK 270
Cdd:PRK13508 240 IPKIEVVNPVGSGDSTVAGIASGLLHQEDDADLLK 274
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
2-280 |
1.25e-30 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 116.81 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 2 IYTVTLNPSIDYIVRLDQVKVGSVNRMDSDDKFAGGKGINVSRVLKRLNIPNTATGFIGGFTGKFITDTLAEEEIETRFV 81
Cdd:PRK10294 4 IYTLTLAPSLDSATITPQIYPEGKLRCSAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPVATV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 82 QVAEDTRINVKIKADQETE---INGTGPTVESVQLEELKAILSSLTAEDTVVFAGSSAKNLGNVIYKDLISLTRQTGAQV 158
Cdd:PRK10294 84 EAKDWTRQNLHVHVEASGEqyrFVMPGAALNEDEFRQLEEQVLEIESGAILVISGSLPPGVKLEKLTQLISAAQKQGIRC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 159 VCDFEGQTLIDSLDYQPL-LVKPNNHELGAIFGVKLESLDEIEKYARELLAKG-AQNVIISMAGDGALLVTSDGAYFAKP 236
Cdd:PRK10294 164 IIDSSGDALSAALAIGNIeLVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGkAKRVVVSLGPQGALGVDSENCIQVVP 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 926808626 237 IKGTVKNSVGAGDSMVAGFTGEFVKSKDAVEAFKWGVACGTATT 280
Cdd:PRK10294 244 PPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAAT 287
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
11-280 |
6.05e-27 |
|
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440290 [Multi-domain] Cd Length: 301 Bit Score: 106.89 E-value: 6.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 11 IDYIVRLDQV-KVGSVNRMDSDDKFAGGKGINVSRVLKRLNIPntaTGFIG----GFTGKFITDTLAEEEIETRFVQVAE 85
Cdd:COG0524 10 VDLVARVDRLpKGGETVLAGSFRRSPGGAAANVAVALARLGAR---VALVGavgdDPFGDFLLAELRAEGVDTSGVRRDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 86 DTRI---NVKIKADQETEINGTGPTVESVQLEELKAILssLTAEDTVVFAGSS-AKNLGNVIYKDLISLTRQTGAQVVCD 161
Cdd:COG0524 87 GAPTglaFILVDPDGERTIVFYRGANAELTPEDLDEAL--LAGADILHLGGITlASEPPREALLAALEAARAAGVPVSLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 162 FeGQTLIDSLDYQPLL---------VKPNNHELGAIFGvklesLDEIEKYARELLAKGAQNVIISMAGDGALLVTSDGAY 232
Cdd:COG0524 165 P-NYRPALWEPARELLrellalvdiLFPNEEEAELLTG-----ETDPEEAAAALLARGVKLVVVTLGAEGALLYTGGEVV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 926808626 233 FAKPIKGTVKNSVGAGDSMVAGFTGEFVKSKDAVEAFKWGVACGTATT 280
Cdd:COG0524 239 HVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVV 286
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
11-280 |
1.52e-17 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 81.06 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 11 IDYIVRLDQV-KVGSVNRMDSDDKFAGGKGINVSRVLKRLNIPNTATGFIG--GFtGKFITDTLAEEEIETRFVQVAEDT 87
Cdd:cd01174 10 VDLVTRVDRLpKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGddAF-GDELLENLREEGIDVSYVEVVVGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 88 R-----INVKikADQETEI------NGTGPTVESVQLEEL----KAILSSL-TAEDTVVFAgssaknlgnviykdlISLT 151
Cdd:cd01174 89 PtgtavITVD--ESGENRIvvvpgaNGELTPADVDAALELiaaaDVLLLQLeIPLETVLAA---------------LRAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 152 RQTGAQVVcdF-------EGQTLIDSLDYqplLVkPNNHELGAIFGVKLESLDEIEKYARELLAKGAQNVIISMAGDGAL 224
Cdd:cd01174 152 RRAGVTVI--LnpaparpLPAELLALVDI---LV-PNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGAL 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 926808626 225 LVTSDGAYFAKPIKGTVKNSVGAGDSMVAGFTGEFVKSKDAVEAFKWGVACGTATT 280
Cdd:cd01174 226 LASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSV 281
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
119-260 |
1.87e-15 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 73.28 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 119 ILSSLTAEdtVVFAGSSA-----KNLGNVIYKDLISLTRQTGAQVVCDF-------EGQTLIDSLDYqPLLVKPNNHELG 186
Cdd:cd00287 45 ALARLGVS--VTLVGADAvvisgLSPAPEAVLDALEEARRRGVPVVLDPgpravrlDGEELEKLLPG-VDILTPNEEEAE 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 926808626 187 AIFGVKLESLDEIEKYARELLAKGAQNVIISMAGDGALLVTSDGAYF-AKPIKGTVKNSVGAGDSMVAGFTGEFV 260
Cdd:cd00287 122 ALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVhVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
116-279 |
8.25e-13 |
|
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238916 [Multi-domain] Cd Length: 288 Bit Score: 67.34 E-value: 8.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 116 LKAILSSLTAEDTVVFAGssakNLGNVIYKDLISLTRQTGAQVVCD----------FEgqtLIDSLDYqpllVKPNNHEL 185
Cdd:cd01941 119 LRKIREALKEAKPIVVDA----NLPEEALEYLLALAAKHGVPVAFEptsapklkklFY---LLHAIDL----LTPNRAEL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 186 GAIFGVKLESLDEIEKYARELLAKGAQNVIISMAGDGALLVTSDGA----YFAKPIKGTVKNSVGAGDSMVAGFTGEFVK 261
Cdd:cd01941 188 EALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGvetkLFPAPQPETVVNVTGAGDAFVAGLVAGLLE 267
|
170
....*....|....*...
gi 926808626 262 SKDAVEAFKWGVACGTAT 279
Cdd:cd01941 268 GMSLDDSLRFAQAAAALT 285
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
33-280 |
2.28e-12 |
|
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
Pssm-ID: 238572 [Multi-domain] Cd Length: 295 Bit Score: 66.12 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 33 KFAGGKGINVSRVLKRLNIPntaTGFIGG----FTGKFITDTLAEEEIETRFVQVAED--TRI-NVKIKADQETEINGTG 105
Cdd:cd01167 25 KAPGGAPANVAVALARLGGK---AAFIGKvgddEFGDFLLETLKEAGVDTRGIQFDPAapTTLaFVTLDADGERSFEFYR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 106 PTVESVQLEElkAILSSLTAEDTVVFAGSSA---KNLGNVIYKdLISLTRQTGAQVVCD------FEGQTLIDSLDYQPL 176
Cdd:cd01167 102 GPAADLLLDT--ELNPDLLSEADILHFGSIAlasEPSRSALLE-LLEAAKKAGVLISFDpnlrppLWRDEEEARERIAEL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 177 L-----VKPNNHELGAIFGvklesLDEIEKYARELLAKGAQNVIISMAGDGALLVTSDGAYFAKPIKGTVKNSVGAGDSM 251
Cdd:cd01167 179 LeladiVKLSDEELELLFG-----EEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTTGAGDAF 253
|
250 260 270
....*....|....*....|....*....|....*.
gi 926808626 252 VAGFTGEFVKSKD-------AVEAFKWGVACGTATT 280
Cdd:cd01167 254 VAGLLAQLLSRGLlaldedeLAEALRFANAVGALTC 289
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
31-279 |
2.88e-12 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 65.53 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 31 DDKFAGGKGINVSRVLKRLNIPNTATGFIGGFT-GKFITDTLAEEEIETRFVQVAEDtrinvkIKADQETEINGT----G 105
Cdd:PRK09813 18 GKAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDyGTKLKQDLARMGVDISHVHTKHG------VTAQTQVELHDNdrvfG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 106 PTVESVqLEELKAI---LSSLTAEDTVVFA--GSSAKNLGNViykdlisltRQTGAQVVCDFEGQ-------TLIDSLDY 173
Cdd:PRK09813 92 DYTEGV-MADFALSeedYAWLAQYDIVHAAiwGHAEDAFPQL---------HAAGKLTAFDFSDKwdsplwqTLVPHLDY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 174 qpllvkpnnhelgaIFGVKLESLDEIEKYARELLAKGAQNVIISMAGDGALlvTSDGAYFAK--PIKGTVKNSVGAGDSM 251
Cdd:PRK09813 162 --------------AFASAPQEDEFLRLKMKAIVARGAGVVIVTLGENGSI--AWDGAQFWRqaPEPVTVVDTMGAGDSF 225
|
250 260
....*....|....*....|....*...
gi 926808626 252 VAGFTGEFVKSKDAVEAFKWGVACGTAT 279
Cdd:PRK09813 226 IAGFLCGWLAGMTLPQAMAQGTACAAKT 253
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
15-276 |
2.96e-12 |
|
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.
Pssm-ID: 238571 [Multi-domain] Cd Length: 294 Bit Score: 65.68 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 15 VRLDQVKVGSVNRMDSDDKFAGGKGINVSRVLKRLNIPntaTGFIGGF----TGKFITDTLAEEEIETRFVQVAEDTRIN 90
Cdd:cd01166 10 VDLSPPGGGRLEQADSFRKFFGGAEANVAVGLARLGHR---VALVTAVgddpFGRFILAELRREGVDTSHVRVDPGRPTG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 91 VKIKadqETEINGTGP-------------TVESVQLEELKAIlssltaeDTVVFAGSSAKNLGNV--IYKDLISLTRQTG 155
Cdd:cd01166 87 LYFL---EIGAGGERRvlyyragsaasrlTPEDLDEAALAGA-------DHLHLSGITLALSESAreALLEALEAAKARG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 156 AQVVCDF----------EGQTLIDSLDYQPLLVKPNNHELGAIFGvkLESLDEIEKYARELLAkGAQNVIISMAGDGALL 225
Cdd:cd01166 157 VTVSFDLnyrpklwsaeEAREALEELLPYVDIVLPSEEEAEALLG--DEDPTDAAERALALAL-GVKAVVVKLGAEGALV 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 926808626 226 VTSDGAYFAKPIKGTVKNSVGAGDSMVAGFTGEFVKSKDAVEAFKWGVACG 276
Cdd:cd01166 234 YTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAA 284
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
5-276 |
8.31e-11 |
|
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]
Pssm-ID: 275175 [Multi-domain] Cd Length: 309 Bit Score: 61.46 E-value: 8.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 5 VTLNPSiDYIVRLDQVKvgsvnrmdSDDKFAGGKGINVSRVLKRLNIpntATGFIGGFT----GKFITDTLAEEEIETRF 80
Cdd:TIGR04382 12 VDLYPQ-QIGVPLEDVT--------SFAKYLGGSPANIAVGAARLGL---KTAFITRVGddqfGRFVRDYLRREGVDTSH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 81 VQVAEDTRINV---KIK--------------ADQETEINgtgpTVESVQLEELKAILSSLTAedtvvFAGSSAKNlgnVI 143
Cdd:TIGR04382 80 VVTDPGRRTSLvflEIKppdefpllfyrenaADLALTPD----DVDEDYIASARALLVSGTA-----LSQEPSRE---AV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 144 YKdLISLTRQTGAQVVCDfegqtlidsLDYQPLLVKPNNH------ELGAIFGVKLESLDEI---------EKYARELLA 208
Cdd:TIGR04382 148 LK-ALEYARAAGVRVVLD---------IDYRPYLWKSPEEagiylrLVLPLVDVIIGTREEFdiaggegddEAAARALLD 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 926808626 209 KGAQNVIISMAGDGALLVTSDGAYF-AKPIKGTVKNSVGAGDSMVAGFTGEFVKSKDAVEAFKWGVACG 276
Cdd:TIGR04382 218 AGVEILVVKRGPEGSLVYTGDGEGVeVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACG 286
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
178-277 |
8.92e-09 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 55.76 E-value: 8.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 178 VKPNNHELGAIFGVKLESLDEIEKYARELLAKGAQNVIISMAGDGALLVTSDGAY-FAKPIKGTVKNSVGAGDSMVAGFT 256
Cdd:PRK09850 184 LKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDISGESgWSAPIKTNVINVTGAGDAMMAGLA 263
|
90 100
....*....|....*....|.
gi 926808626 257 GEFVKSKDAVEAFKWGVACGT 277
Cdd:PRK09850 264 SCWVDGMPFAESVRFAQGCSS 284
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
32-256 |
4.17e-08 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 53.33 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 32 DKFAGGKGiNVSRVLKRLNIPNTATGFIGGFT-GKFITDTLAEEEIETRFVQVAE-----DTRI---NVKI-KADQETEi 101
Cdd:cd01172 36 EIRLGGAA-NVANNLASLGAKVTLLGVVGDDEaGDLLRKLLEKEGIDTDGIVDEGrptttKTRViarNQQLlRVDREDD- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 102 ngtGPTVESVQLEELKAILSSLTAEDTVVFagsSAKNLG----NVIyKDLISLTRQTGAQVVCD--------FEGQTLId 169
Cdd:cd01172 114 ---SPLSAEEEQRLIERIAERLPEADVVIL---SDYGKGvltpRVI-EALIAAARELGIPVLVDpkgrdyskYRGATLL- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 170 sldyqpllvKPNNHELGAIFGVKLESLDEIEKYARELLAK-GAQNVIISMAGDGALLVTSDGAYFAKPIKGT-VKNSVGA 247
Cdd:cd01172 186 ---------TPNEKEAREALGDEINDDDELEAAGEKLLELlNLEALLVTLGEEGMTLFERDGEVQHIPALAKeVYDVTGA 256
|
....*....
gi 926808626 248 GDSMVAGFT 256
Cdd:cd01172 257 GDTVIATLA 265
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
177-269 |
1.15e-07 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 52.18 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 177 LVKPNNHELGAIFGVKLESLDEIEKYARELLAKGAQNVII-------SMAGD-GALLVTSDGAYFAK-PIKGTVKNSVGA 247
Cdd:PRK05756 141 IITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVtslaragYPADRfEMLLVTADGAWHISrPLVDFMRQPVGV 220
|
90 100
....*....|....*....|..
gi 926808626 248 GDSMVAGFTGEFVKSKDAVEAF 269
Cdd:PRK05756 221 GDLTSALFLARLLQGGSLEEAL 242
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
193-279 |
1.11e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 49.83 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 193 LESLDEI---EKYARELLAKG--AQNVIISMAGDGALLVTSDGAYFAKPIKGTVKNSVGAGDSMVAGFTGEFVKSKDAVE 267
Cdd:PLN02341 296 AEALTGIrnpILAGQELLRPGirTKWVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAAAIALGYIHNLPLVN 375
|
90
....*....|..
gi 926808626 268 AFKWGVACGTAT 279
Cdd:PLN02341 376 TLTLANAVGAAT 387
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
181-276 |
1.26e-06 |
|
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.
Pssm-ID: 238573 [Multi-domain] Cd Length: 312 Bit Score: 49.15 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 181 NNHELGAIFGVKLESLDEIekyARELLAKGAQNVIISMAGDGALLVTSDGAYFAKPIK-GTVKNSVGAGDSMVAGFTGEF 259
Cdd:cd01168 207 NEEEAEALAEAETTDDLEA---ALKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPvEKIVDTNGAGDAFAGGFLYGL 283
|
90
....*....|....*..
gi 926808626 260 VKSKDAVEAFKWGVACG 276
Cdd:cd01168 284 VQGEPLEECIRLGSYAA 300
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
34-279 |
1.63e-06 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 48.50 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 34 FAGGKGINVSRVLKRLNIPntaTGFIGGF----TGKFITDTLAEEEIETRFVQVAED----TRINVKiKADQETEINGTG 105
Cdd:cd01940 20 YPGGNALNVAVYAKRLGHE---SAYIGAVgnddAGAHVRSTLKRLGVDISHCRVKEGenavADVELV-DGDRIFGLSNKG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 106 PTVESVQLEELKAILSSLTAEDTVVFA--GSSAKNLGNVIYkdlisltrqTGAQVVCDF-------EGQTLIDSLDYqpl 176
Cdd:cd01940 96 GVAREHPFEADLEYLSQFDLVHTGIYSheGHLEKALQALVG---------AGALISFDFsdrwdddYLQLVCPYVDF--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 177 lvkpnnhelgAIFGVKLESLDEIEKYARELLAKGAQNVIISMAGDGALLvtSDGAYFAK--PIKGTVKNSVGAGDSMVAG 254
Cdd:cd01940 164 ----------AFFSASDLSDEEVKAKLKEAVSRGAKLVIVTRGEDGAIA--YDGAVFYSvaPRPVEVVDTLGAGDSFIAG 231
|
250 260
....*....|....*....|....*.
gi 926808626 255 FTGEFVKSKDAV-EAFKWGVACGTAT 279
Cdd:cd01940 232 FLLSLLAGGTAIaEAMRQGAQFAAKT 257
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
165-274 |
3.78e-05 |
|
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.
Pssm-ID: 430062 [Multi-domain] Cd Length: 246 Bit Score: 44.01 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 165 QTLIDSLDYQPLLVKPNNHELGAIFGVKLESLDEIEKYARELLAKGAQNVII---SMAGDGA----LLVTSDGAY-FAKP 236
Cdd:pfam08543 110 EALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIkggHLEGEEAvvtdVLYDGGGFYtLEAP 189
|
90 100 110
....*....|....*....|....*....|....*...
gi 926808626 237 iKGTVKNSVGAGDSMVAGFTGEFVKSKDAVEAFKWGVA 274
Cdd:pfam08543 190 -RIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKE 226
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
11-267 |
4.76e-05 |
|
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238919 [Multi-domain] Cd Length: 289 Bit Score: 44.34 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 11 IDYIVRLDQV-KVGSVNRMDSDDKFAGGkGINVSRVLKRLNIPNTATGFIG-GFTGKFITDTLAEEEIETRF-VQVAEDT 87
Cdd:cd01944 10 VDIVLDVDKLpASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGnGNWADQIRQAMRDEGIEILLpPRGGDDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 88 -RINVKIKADQE-TEINGTGptVESV-QLEELKAIlsSLTAEDTVVFAGSS--AKNLGNVIYKDLIsLTRQTGAQVVCDF 162
Cdd:cd01944 89 gCLVALVEPDGErSFISISG--AEQDwSTEWFATL--TVAPYDYVYLSGYTlaSENASKVILLEWL-EALPAGTTLVFDP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 163 egQTLIDSLDYQPL--LVKPN-----NHELGAIFGVKLESldEIEKYARELLAKGAQNVIISMAGDGALLVTSDGAYFAK 235
Cdd:cd01944 164 --GPRISDIPDTILqaLMAKRpiwscNREEAAIFAERGDP--AAEASALRIYAKTAAPVVVRLGSNGAWIRLPDGNTHII 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 926808626 236 P-IKGTVKNSVGAGDSMVAGFTGEFVKS---KDAVE 267
Cdd:cd01944 240 PgFKVKAVDTIGAGDTHAGGMLAGLAKGmslADAVL 275
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
177-275 |
5.23e-05 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 44.34 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 177 LVKPNNHELGAIFGVKLESLDEIEKYARELLAKGAQNVIISMAGDGALLVTSD-GAYFAKPIKGTVKNSVGAGDSMVAGF 255
Cdd:PTZ00292 201 LFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEKEnEPVHVPGKRVKAVDTTGAGDCFVGSM 280
|
90 100
....*....|....*....|
gi 926808626 256 TGEFVKSKDAVEAFKWGVAC 275
Cdd:PTZ00292 281 AYFMSRGKDLKESCKRANRI 300
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
201-268 |
6.89e-05 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 43.61 E-value: 6.89e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 201 KYARELLAKGAQNVIISMAGDGALLVTSDGAYF--AKPIKgTVKNSVGAGDSMVAGFTGEFVKSKDAVEA 268
Cdd:cd01946 185 KAARLILAMGPKALIIKRGEYGALLFTDDGYFAapAYPLE-SVFDPTGAGDTFAGGFIGYLASQKDTSEA 253
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
160-278 |
1.88e-04 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 42.33 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 160 CDFE-GQTLIDSLDYQPLLvKPNNHELGAIFGVKL--ESLDEIEKYARELL-----AKGAQNVIISMAG-DGALLVTSDG 230
Cdd:cd01943 166 CDPEnLEDLLQALPRVDVF-SPNLEEAARLLGLPTsePSSDEEKEAVLQALlfsgiLQDPGGGVVLRCGkLGCYVGSADS 244
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 926808626 231 -------AYFAKPIKgtVKNSVGAGDSMVAGFTGEFVKSKDAVEAFKWG-VACGTA 278
Cdd:cd01943 245 gpelwlpAYHTKSTK--VVDPTGGGNSFLGGFAAGLALTKSIDEACIYGsVAASFA 298
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
169-270 |
2.18e-04 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 41.88 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 169 DSLDYQPLLVKPNNHELGAIFGVKLESLDEIEKYARELLAKGAQNVII----SMAGDGALLVTSDGAYF----AKPIKGT 240
Cdd:PRK12412 127 DVLVPKALVVTPNLFEAYQLSGVKINSLEDMKEAAKKIHALGAKYVLIkggsKLGTETAIDVLYDGETFdlleSEKIDTT 206
|
90 100 110
....*....|....*....|....*....|
gi 926808626 241 vkNSVGAGDSMVAGFTGEFVKSKDAVEAFK 270
Cdd:PRK12412 207 --NTHGAGCTYSAAITAELAKGKPVKEAVK 234
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
177-268 |
3.15e-04 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 41.62 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 177 LVKPNNHELgaifgVKLESLDEIEKYARELLAKgaqNVIISMAGDGALLVTSDGAYFAKPIKGTVKNSVGAGDSMVAGFT 256
Cdd:cd01937 158 VLKLSRVEA-----EVISTPTELARLIKETGVK---EIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGDVFLAAFL 229
|
90
....*....|..
gi 926808626 257 GEFVKSKDAVEA 268
Cdd:cd01937 230 YSRLSGKDIKEA 241
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
180-276 |
4.02e-04 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 41.14 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 180 PNNHELGAIfgVKLESLDEIEkyarelLAKGAQNVIISMAGDGALLVTSDGAYFAKPIKGT-VKNSVGAGDSMVAGFTGE 258
Cdd:cd01942 180 VNDYEAELL--KERTGLSEAE------LASGVRVVVVTLGPKGAIVFEDGEEVEVPAVPAVkVVDTTGAGDAFRAGFLYG 251
|
90
....*....|....*...
gi 926808626 259 FVKSKDAVEAFKWGVACG 276
Cdd:cd01942 252 LLRGYDLEESLRLGNLAA 269
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
198-276 |
8.16e-04 |
|
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238922 [Multi-domain] Cd Length: 265 Bit Score: 40.09 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 198 EIEKYARELLAKGAQNVIISMAGDGALLVTSdGAYFA-KPIKGTVKNSVGAGDSMVAGFTGEFVKSKDAVEAFKWGVACG 276
Cdd:cd01947 177 GELVVAEKIAGPFPRYLIVTEGELGAILYPG-GRYNHvPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCG 255
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
178-275 |
6.35e-03 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 37.99 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926808626 178 VKPNNHELGAIFGVKLESLDEIEKYARELLAKGAQNVIISMAGDGALLVTSDGAYFA-KPIKGTVKNSVGAGDSMVAGFT 256
Cdd:PRK09954 237 LKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSEKDGEQFLlTAPAHTTVDSFGADDGFMAGLV 316
|
90
....*....|....*....
gi 926808626 257 GEFVKSKDAVEAFKWGVAC 275
Cdd:PRK09954 317 YSFLEGYSFRDSARFAMAC 335
|
|
| |
